Unknown

Dataset Information

0

Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch.


ABSTRACT: Significant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed Watson-Crick and Hoogsteen A•U pair formation. The bound fluoride ion is encapsulated within the junctional architecture, anchored in place through direct coordination to three Mg(2+) ions, which in turn are octahedrally coordinated to water molecules and five inwardly pointing backbone phosphates. Our structure of the fluoride riboswitch in the bound state shows how RNA can form a binding pocket selective for fluoride, while discriminating against larger halide ions. The T. petrophila fluoride riboswitch probably functions in gene regulation through a transcription termination mechanism.

SUBMITTER: Ren A 

PROVIDER: S-EPMC3744881 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

altmetric image

Publications

Fluoride ion encapsulation by Mg2+ ions and phosphates in a fluoride riboswitch.

Ren Aiming A   Rajashankar Kanagalaghatta R KR   Patel Dinshaw J DJ  

Nature 20120513 7401


Significant advances in our understanding of RNA architecture, folding and recognition have emerged from structure-function studies on riboswitches, non-coding RNAs whose sensing domains bind small ligands and whose adjacent expression platforms contain RNA elements involved in the control of gene regulation. We now report on the ligand-bound structure of the Thermotoga petrophila fluoride riboswitch, which adopts a higher-order RNA architecture stabilized by pseudoknot and long-range reversed W  ...[more]

Similar Datasets

| S-EPMC5314772 | biostudies-literature
| S-EPMC3102267 | biostudies-literature
| S-EPMC6641604 | biostudies-literature
| S-EPMC2526249 | biostudies-literature
| S-EPMC5861836 | biostudies-other
| S-EPMC3507322 | biostudies-literature
| S-EPMC3845237 | biostudies-literature
| S-EPMC7362733 | biostudies-literature
| S-EPMC6614840 | biostudies-literature
| S-EPMC3562059 | biostudies-literature